Inhibition of lytic polysaccharide monooxygenase by natural plant extracts

Research output: Contribution to journalJournal articlepeer-review

Standard

Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. / Tokin, Radina; Frandsen, Kristian E. H.; Ipsen, Johan Ørskov; Lo Leggio, Leila; Poojary, Mahesha M.; Berrin, Jean-Guy; Grisel, Sacha; Brander, Søren; Jensen, Poul Erik; Johansen, Katja Salomon.

In: New Phytologist, Vol. 232, No. 3, 2021, p. 1337–1349.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Tokin, R, Frandsen, KEH, Ipsen, JØ, Lo Leggio, L, Poojary, MM, Berrin, J-G, Grisel, S, Brander, S, Jensen, PE & Johansen, KS 2021, 'Inhibition of lytic polysaccharide monooxygenase by natural plant extracts', New Phytologist, vol. 232, no. 3, pp. 1337–1349. https://doi.org/10.1111/nph.17676

APA

Tokin, R., Frandsen, K. E. H., Ipsen, J. Ø., Lo Leggio, L., Poojary, M. M., Berrin, J-G., Grisel, S., Brander, S., Jensen, P. E., & Johansen, K. S. (2021). Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. New Phytologist, 232(3), 1337–1349. https://doi.org/10.1111/nph.17676

Vancouver

Tokin R, Frandsen KEH, Ipsen JØ, Lo Leggio L, Poojary MM, Berrin J-G et al. Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. New Phytologist. 2021;232(3):1337–1349. https://doi.org/10.1111/nph.17676

Author

Tokin, Radina ; Frandsen, Kristian E. H. ; Ipsen, Johan Ørskov ; Lo Leggio, Leila ; Poojary, Mahesha M. ; Berrin, Jean-Guy ; Grisel, Sacha ; Brander, Søren ; Jensen, Poul Erik ; Johansen, Katja Salomon. / Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. In: New Phytologist. 2021 ; Vol. 232, No. 3. pp. 1337–1349.

Bibtex

@article{6bfa107933b840cfad66d04de128fc10,
title = "Inhibition of lytic polysaccharide monooxygenase by natural plant extracts",
abstract = "Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported.In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC–MS, we successfully identified a natural LPMO inhibitor.Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC–MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1.The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts.",
keywords = "Cinnamomum cassia, cinnamtannin B1, inhibitor, Lentinus similis, LPMO, lytic polysaccharide monooxygenase, plant extract",
author = "Radina Tokin and Frandsen, {Kristian E. H.} and Ipsen, {Johan {\O}rskov} and {Lo Leggio}, Leila and Poojary, {Mahesha M.} and Jean-Guy Berrin and Sacha Grisel and S{\o}ren Brander and Jensen, {Poul Erik} and Johansen, {Katja Salomon}",
year = "2021",
doi = "10.1111/nph.17676",
language = "English",
volume = "232",
pages = "1337–1349",
journal = "New Phytologist",
issn = "0028-646X",
publisher = "Academic Press",
number = "3",

}

RIS

TY - JOUR

T1 - Inhibition of lytic polysaccharide monooxygenase by natural plant extracts

AU - Tokin, Radina

AU - Frandsen, Kristian E. H.

AU - Ipsen, Johan Ørskov

AU - Lo Leggio, Leila

AU - Poojary, Mahesha M.

AU - Berrin, Jean-Guy

AU - Grisel, Sacha

AU - Brander, Søren

AU - Jensen, Poul Erik

AU - Johansen, Katja Salomon

PY - 2021

Y1 - 2021

N2 - Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported.In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC–MS, we successfully identified a natural LPMO inhibitor.Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC–MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1.The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts.

AB - Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported.In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC–MS, we successfully identified a natural LPMO inhibitor.Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC–MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1.The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts.

KW - Cinnamomum cassia

KW - cinnamtannin B1

KW - inhibitor

KW - Lentinus similis

KW - LPMO

KW - lytic polysaccharide monooxygenase

KW - plant extract

U2 - 10.1111/nph.17676

DO - 10.1111/nph.17676

M3 - Journal article

C2 - 34389999

VL - 232

SP - 1337

EP - 1349

JO - New Phytologist

JF - New Phytologist

SN - 0028-646X

IS - 3

ER -

ID: 276232301